4PHC
Crystal Structure of a human cytosolic histidyl-tRNA synthetase, histidine-bound
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004821 | molecular_function | histidine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006427 | biological_process | histidyl-tRNA aminoacylation |
| A | 0032543 | biological_process | mitochondrial translation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004821 | molecular_function | histidine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006427 | biological_process | histidyl-tRNA aminoacylation |
| B | 0032543 | biological_process | mitochondrial translation |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0003723 | molecular_function | RNA binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004821 | molecular_function | histidine-tRNA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005829 | cellular_component | cytosol |
| C | 0006412 | biological_process | translation |
| C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| C | 0006427 | biological_process | histidyl-tRNA aminoacylation |
| C | 0032543 | biological_process | mitochondrial translation |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0003723 | molecular_function | RNA binding |
| D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| D | 0004821 | molecular_function | histidine-tRNA ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005829 | cellular_component | cytosol |
| D | 0006412 | biological_process | translation |
| D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| D | 0006427 | biological_process | histidyl-tRNA aminoacylation |
| D | 0032543 | biological_process | mitochondrial translation |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue HIS A 1001 |
| Chain | Residue |
| A | ASP130 |
| A | TYR331 |
| A | GLY360 |
| A | TYR363 |
| A | GLY381 |
| A | LEU382 |
| A | SER383 |
| A | HOH1113 |
| A | THR132 |
| A | ARG157 |
| A | GLN173 |
| A | ASP175 |
| A | ASP177 |
| A | ARG326 |
| A | LEU328 |
| A | TYR330 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 1002 |
| Chain | Residue |
| A | ASN146 |
| B | TYR454 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue HIS B 1001 |
| Chain | Residue |
| B | ASP130 |
| B | THR132 |
| B | ARG157 |
| B | GLN173 |
| B | ASP175 |
| B | ASP177 |
| B | ARG326 |
| B | TYR330 |
| B | TYR331 |
| B | GLY360 |
| B | TYR363 |
| B | GLY381 |
| B | LEU382 |
| B | HOH1116 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 1002 |
| Chain | Residue |
| A | TYR454 |
| B | ASN146 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue HIS C 1001 |
| Chain | Residue |
| C | ASP130 |
| C | THR132 |
| C | ARG157 |
| C | GLN173 |
| C | ASP175 |
| C | ASP177 |
| C | ARG326 |
| C | LEU328 |
| C | TYR330 |
| C | TYR331 |
| C | TYR363 |
| C | GLY381 |
| C | LEU382 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue GOL C 1002 |
| Chain | Residue |
| C | ASN146 |
| D | TYR454 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 1003 |
| Chain | Residue |
| C | TYR454 |
| D | GLU90 |
| D | ASN146 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue HIS D 1001 |
| Chain | Residue |
| D | ASP130 |
| D | THR132 |
| D | ARG157 |
| D | GLN173 |
| D | ASP175 |
| D | ASP177 |
| D | ARG326 |
| D | TYR330 |
| D | TYR331 |
| D | GLY360 |
| D | GLY381 |
| D | LEU382 |
| D | SER383 |
| D | HOH1109 |
Functional Information from PROSITE/UniProt
| site_id | PS00762 |
| Number of Residues | 29 |
| Details | WHEP_TRS_1 WHEP-TRS domain signature. QGErVRglKqqKAsaelIEeeVakLlklK |
| Chain | Residue | Details |
| A | GLN14-LYS42 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25151410, ECO:0007744|PDB:4PHC |
| Chain | Residue | Details |
| C | ARG326 | |
| C | TYR330 | |
| D | ASP130 | |
| D | ARG157 | |
| D | GLN173 | |
| D | ASP177 | |
| D | ARG326 | |
| D | TYR330 | |
| A | ASP130 | |
| A | ARG157 | |
| A | GLN173 | |
| A | ASP177 | |
| A | ARG326 | |
| A | TYR330 | |
| B | ASP130 | |
| B | ARG157 | |
| B | GLN173 | |
| B | ASP177 | |
| B | ARG326 | |
| B | TYR330 | |
| C | ASP130 | |
| C | ARG157 | |
| C | GLN173 | |
| C | ASP177 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 | |
| C | ALA2 | |
| D | ALA2 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99KK9 |
| Chain | Residue | Details |
| A | SER66 | |
| B | SER66 | |
| C | SER66 | |
| D | SER66 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER356 | |
| B | SER356 | |
| C | SER356 | |
| D | SER356 |
